ID A0A167KFI4_CALVF Unreviewed; 1096 AA.
AC A0A167KFI4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=CALVIDRAFT_599670 {ECO:0000313|EMBL:KZO94593.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO94593.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO94593.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO94593.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000006};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV417293; KZO94593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167KFI4; -.
DR STRING; 1330018.A0A167KFI4; -.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR InterPro; IPR034300; PNTB-like.
DR NCBIfam; TIGR00561; pntA; 1.
DR PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF02233; PNTB; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 518..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 691..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..225
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 234..400
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1096 AA; 114134 MW; 6E00CBA1C13503A8 CRC64;
MGHLDSFSDK LTSNECPALS QGGSEHATIP YPARHAPYSL SNFDWRLTRI CLSAAVLLRA
FHRSPIAWAE PTATPTGTPY AKLTVGVPLE TFPDERRVAL TPQNTVALLK KGFGRVLVES
GAGREAQFLD EQYKAAGATI VSRDELYAGT DILLKVRPPV LGQSGTDVDK LKKDSTLISF
LYPAQNKPLI EALAKKEINA LAMDCIPRVS RAQVFDALSS MANIAGYKAV LEAANHFGRF
LTGQTTAAGK IPPCKVLVIG AGVAGLSAIA TARRMGAITR GFDTRAVARE QVESLGAEFL
EVTGVAEDGA GAGGYAKVMS KEFIEKEMEL FMEQCRNNVD IVITTALIPG KPAPKLITKE
MVAAMKQGSV IVDLAAEAGG NCELTQPGKV IHHNGVTIIG YTDLPSRLPT QASTLYSNNI
TKFLLSISSD PGYFNIDHSD NVVRGALILE KGSLMWPPPP SAVAAPPPPP PKIEAKKEEV
TAITPWQQAT RDVAVTTAGM GGILALGKAT GTAFMDNFFT FGLASLIGYR VVWGVAPALH
SPLMSVTNAI SGMVAIGGLF VMGGGYFPGT IPQVLGAMSV ALAFVNIFGG FVVTQRMLDM
FKRPTDPPEY AWLNLVPAVV FTGGFIASAA TGMSGLVQAG YLASSVLCIG ALSGLGSQST
ARQGNAFGIL GVGSGILASL GAVGFPTPVL AQFGAVAGIG AVAGTWIGRR ITGTDLPQTV
AALHSVVGLA AVLTSIGSVL ADLSHVTTLH MVTAYLGVLI GGITFTGSIV AFLKLAGKMS
SKPVILPGRH LINGGMLAAN LGLMAPFLSA GPGAPLIAAG CLIANAGLSF AKGWTLTSAV
GGADMPVCIT VLNSYSGFAL VAEGLMLENP LLTTVGSLIG VSGGILSYIM CRAMNRSLTN
VLFGGIPPMP ASADGPTITG TVTPTNVEET VEALLNADNV IITPGYGMAV AKAQFTVAEI
TKALTAKGVK VRFGVHPVAG RMPGQLNVLL AEASVPYDVV LEMEEINEDF SDTDVVLVIG
ANDTVNPIAL EPGSSIAGMP VLHVWQAKQV IVMKRSMSSG YADVPNPLFY MPNTRMLFGD
AKDTCDAIKK AIDEKA
//
